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http://purl.uniprot.org/citations/12505993http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12505993http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12505993http://www.w3.org/2000/01/rdf-schema#comment"Type IIA and type IIB topoisomerases each possess the ability to pass one DNA duplex through another in an ATP-dependent manner. The role of ATP in the strand passage reaction is poorly understood, particularly for the type IIB (topoisomerase VI) family. We have solved the structure of the ATP-binding subunit of topoisomerase VI (topoVI-B) in two states: an unliganded monomer and a nucleotide-bound dimer. We find that topoVI-B is highly structurally homologous to the entire 40-43 kDa ATPase region of type IIA topoisomerases and MutL proteins. Nucleotide binding to topoVI-B leads to dimerization of the protein and causes dramatic conformational changes within each protomer. Our data demonstrate that type IIA and type IIB topoisomerases have descended from a common ancestor and reveal how ATP turnover generates structural signals in the reactions of both type II topoisomerase families. When combined with the structure of the A subunit to create a picture of the intact topoisomerase VI holoenzyme, the ATP-driven motions of topoVI-B reveal a simple mechanism for strand passage by the type IIB topoisomerases."xsd:string
http://purl.uniprot.org/citations/12505993http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg008"xsd:string
http://purl.uniprot.org/citations/12505993http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg008"xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/author"Berger J.M."xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/author"Berger J.M."xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/author"Corbett K.D."xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/author"Corbett K.D."xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/pages"151-163"xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/pages"151-163"xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/title"Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution."xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/title"Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution."xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/12505993http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/12505993http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12505993
http://purl.uniprot.org/citations/12505993http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12505993
http://purl.uniprot.org/citations/12505993http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12505993
http://purl.uniprot.org/citations/12505993http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12505993
http://purl.uniprot.org/uniprot/O05207http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12505993
http://purl.uniprot.org/uniprot/O05207#attribution-8B9857992A5B113C0D0F5EBC6D1161A0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12505993